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H3917

Sigma-Aldrich

Heparinase I and III Blend from Flavobacterium heparinum

lyophilized powder, stabilized with ∼ 25% (w/w) bovine serum albumin, ≥200 unit/mg protein (enzyme + BSA)

Synonym(s):

Heparinase I and Heparinase III blend

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About This Item

Enzyme Commission number:
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

bacterial (Flavobacterium heparinum)

Quality Level

conjugate

conjugate (Glucosaminoglycan)

form

lyophilized powder

specific activity

≥200 units/mg protein

concentration

≥200 unit/mg protein (enzyme + BSA)

shipped in

dry ice

storage temp.

−20°C

General description

Heparinase is an inducible, non-extracellular heparin-degrading enzyme. Three types of heparinises are produced by Flavobacterium heparinum and contains specific sequences of heparin.

Application

Heparinase I and III Blend from Flavobacterium heparinum has been used in:
  • the digestion of heparan sulfate from ovine vitreous
  • human embryonic kidney cells
  • glycosaminoglycans from arterial tissues
  • P0 retinae digestion

Biochem/physiol Actions

Heparinase I and III plays vital role in various biological processes: modulate cell-growth factor interactions, cell-lipoprotein interactions, neovascularization. It cleaves highly sulphated polysaccharide chains in presence of 2-O-sulfated α-L-idopyranosyluronic acid and β-D-glucopyranosyluronic acid residues of polysaccharides.
Heparin-degrading lyase that recognizes heparin sulfate proteoglycan as its primary substrate.

Packaging

Sold on the basis of Heparinase I units

Unit Definition

One unit will form 0.1 micromole of unsaturated uronic acid per hour at 7.5 at 25 degrees C using Heparin, Sodium as substrate for heparinase I.

One unit will form 0.1 micromole of unsaturated uronic acid per hour at 7.5 at 25 degrees C using bovine kidney Heparan, Sulfate as substrate for heparinase III.

One unit will form 0.1 μmole of unsaturated uronic acid per hr at pH 7.5 at 25 °C. One International Unit (I.U.) is equivalent to approx. 600 Sigma units. Package sizes are sold in Sigma units.

Other Notes

Enzyme Commission Numbers: 4.2.2.7 Hep I and 4.2.2.8 Hep III

Storage Class Code

13 - Non Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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S Ernst et al.
Critical reviews in biochemistry and molecular biology, 30(5), 387-444 (1995-01-01)
Glycosaminoglycans (GAGs) play an intricate role in the extracellular matrix (ECM), not only as soluble components and polyelectrolytes, but also by specific interactions with growth factors and other transient components of the ECM. Modifications of GAG chains, such as isomerization
Farizeh Aalam et al.
PLoS pathogens, 16(10), e1008968-e1008968 (2020-10-20)
Despite 25 years of research, the basic virology of Kaposi Sarcoma Herpesviruses (KSHV) in B lymphocytes remains poorly understood. This study seeks to fill critical gaps in our understanding by characterizing the B lymphocyte lineage-specific tropism of KSHV. Here, we
P M Galliher et al.
Applied and environmental microbiology, 41(2), 360-365 (1981-02-01)
Heparinase production by Flavobacterium heparinum in complex protein digest medium, with heparin employed as the inducer, has been studied and improved. The maximum productivity of heparinase has been increased 156-fold over that achieved by previously published methods to 375 U/liter
D A Chappell et al.
The Journal of biological chemistry, 268(19), 14168-14175 (1993-07-05)
Bovine milk lipoprotein lipase (LPL) induced binding, uptake, and degradation of 125I-labeled normal human triglyceride-rich lipoproteins by cultured mutant fibroblasts lacking LDL receptors. The induction was dose-dependent and occurred whether LPL and 125I-lipoproteins were added to incubation media simultaneously or
Cassandra R Blanchette et al.
PLoS genetics, 13(1), e1006525-e1006525 (2017-01-10)
The regulation of cell migration is essential to animal development and physiology. Heparan sulfate proteoglycans shape the interactions of morphogens and guidance cues with their respective receptors to elicit appropriate cellular responses. Heparan sulfate proteoglycans consist of a protein core

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